Mercer J F, McAdam W, Chambers G W, Walker I D
Biochem J. 1986 Jun 15;236(3):679-83. doi: 10.1042/bj2360679.
High performance liquid chromatography maps of tryptic and chymotryptic peptides from the W and L forms of rat phenylalanine hydroxylase differed by one peptide. Sequencing of the variant tryptic peptides showed a substitution of threonine in the W form by isoleucine in the L form and this same difference was confirmed in the chymotryptic peptides. This allelic substitution would result from a nucleotide change of ACA to ATA at amino acid position 371 of the full phenylalanine hydroxylase sequence. Altered sodium dodecyl sulphate binding is postulated to explain the change in mobility of the proteins observed on sodium dodecyl sulphate/polyacrylamide gels.
大鼠苯丙氨酸羟化酶W型和L型的胰蛋白酶肽段和糜蛋白酶肽段的高效液相色谱图谱有一个肽段不同。对变异的胰蛋白酶肽段进行测序显示,W型中的苏氨酸在L型中被异亮氨酸取代,并且在糜蛋白酶肽段中也证实了这一相同差异。这种等位基因替代是由完整苯丙氨酸羟化酶序列第371位氨基酸处的ACA核苷酸变为ATA所致。推测十二烷基硫酸钠结合的改变可解释在十二烷基硫酸钠/聚丙烯酰胺凝胶上观察到的蛋白质迁移率变化。